ID   Q0AW13_SYNWW            Unreviewed;       486 AA.
AC   Q0AW13;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   04-NOV-2026, entry version 86.
DE   SubName: Full=Serine phosphatase RsbU regulator of sigma subunit-like protein {ECO:0000313|EMBL:ABI69091.1};
GN   OrderedLocusNames=Swol_1793 {ECO:0000313|EMBL:ABI69091.1};
OS   Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC   Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
OC   Syntrophomonadaceae; Syntrophomonas.
OX   NCBI_TaxID=335541 {ECO:0000313|EMBL:ABI69091.1, ECO:0000313|Proteomes:UP000001968};
RN   [1] {ECO:0000313|Proteomes:UP000001968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2245B / Goettingen {ECO:0000313|Proteomes:UP000001968};
RX   PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA   Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA   McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT   "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT   metabolism and biohydrogen production.";
RL   Environ. Microbiol. 12:2289-2301(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-phospho-L-seryl-[protein] + H2O = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU01082};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-phospho-L-threonyl-[protein] + H2O = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU01082};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU01082};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU01082};
CC       Note=Binds 2 magnesium or manganese ions per subunit.
CC       {ECO:0000256|PROSITE-ProRule:PRU01082};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
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DR   EMBL; CP000448; ABI69091.1; -; Genomic_DNA.
DR   STRING; 335541.Swol_1793; -.
DR   KEGG; swo:Swol_1793; -.
DR   eggNOG; COG2208; Bacteria.
DR   eggNOG; COG3275; Bacteria.
DR   HOGENOM; CLU_606380_0_0_9; -.
DR   OMA; AAMMNKQ; -.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   InterPro; IPR052016; Bact_Sigma-Reg.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   InterPro; IPR011620; Sig_transdc_His_kinase_LytS_TM.
DR   PANTHER; PTHR43156:SF2; STAGE II SPORULATION PROTEIN E; 1.
DR   PANTHER; PTHR43156; STAGE II SPORULATION PROTEIN E-RELATED; 1.
DR   Pfam; PF07694; 5TM-5TMR_LYT; 1.
DR   Pfam; PF07228; SpoIIE; 1.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS51746; PPM_2; 1.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:InterPro.
DR   Proteomes; UP000001968; Chromosome.
DR   AlphaFoldDB; Q0AW13; -.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01082};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01082};
KW   Protein phosphatase {ECO:0000256|PROSITE-ProRule:PRU01082};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001968};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        40..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        79..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        135..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        207..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          267..482
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
SQ   SEQUENCE   486 AA;  53711 MW;  9AD513D2A2DACE58 CRC64;
     MLKLLRSFFR CFKSNFFCFC LNSRRGTVGR CFKISEIIDL LINLIKNMAV IIVLAYVLTR
     TRAFAAMMNK QTMNWRQQAT LILVFGIFSI FGTLSGININ GAIANIRDLG PAIAGLVGGP
     LVGFGAGFIG GLHRYSLGGL TCLPCSVATV LAGLTGGLIS QFKKNEFITI QEAVIFMALF
     EAFHMGLNLI MVKPFDQIYV IIKNVSLPMI FTNALGMGIF VFIIHNLVRE KEMQKQKELI
     ESELTVAREI QMSIIPKIFP PFPERPEFDL FAVLEPAKEV GGDLYDYFLL DDDHLCFTIG
     DVSGKGVPAS LFMAVTKTLI KAKADIRLEP DEILYAVNND LCADNDSGMF VTEFLGILTI
     SSGEIVYSNG GHNLPYILRK EGTIKMLPRM AGMALGVMEE IPYSQARVKL NPGDSLVMYT
     DGVTEAMNDS GELFGEERLE RNLAGITGYT AREEVEVILR STRDFVQEAS QSDDITILVL
     QFIGGK
//